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Yorodumi- PDB-2l9g: Solution structure of AS1p-Tar in 10% negatively charged bicelles -
+Open data
-Basic information
Entry | Database: PDB / ID: 2l9g | ||||||
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Title | Solution structure of AS1p-Tar in 10% negatively charged bicelles | ||||||
Components | Methyl-accepting chemotaxis protein II | ||||||
Keywords | MEMBRANE PROTEIN / HAMP-domain / signal transduction / transmembrane communication / helicity of AS1 / membrane-spanning receptors | ||||||
Function / homology | Function and homology information detection of chemical stimulus / methyl accepting chemotaxis protein complex / protein histidine kinase binding / positive regulation of post-translational protein modification / cell tip / regulation of chemotaxis / signal complex assembly / cellular response to amino acid stimulus / protein homooligomerization / chemotaxis ...detection of chemical stimulus / methyl accepting chemotaxis protein complex / protein histidine kinase binding / positive regulation of post-translational protein modification / cell tip / regulation of chemotaxis / signal complex assembly / cellular response to amino acid stimulus / protein homooligomerization / chemotaxis / transmembrane signaling receptor activity / signal transduction / protein homodimerization activity / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | closest to the average, model 9 | ||||||
Authors | Unnerstale, S. / von Heijne, G. / Draheim, R.R. / Maler, L. | ||||||
Citation | Journal: Biochim.Biophys.Acta / Year: 2011 Title: Structural characterization of AS1-membrane interactions from a subset of HAMP domains Authors: Unnerstale, S. / Maler, L. / Draheim, R.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l9g.cif.gz | 141.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l9g.ent.gz | 100.5 KB | Display | PDB format |
PDBx/mmJSON format | 2l9g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l9/2l9g ftp://data.pdbj.org/pub/pdb/validation_reports/l9/2l9g | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2120.647 Da / Num. of mol.: 1 Fragment: peptide AS1p-Tar from HAMP domain, UNP residues 214-232 Source method: obtained synthetically Details: Obtained from PolyPeptide Group (Strasbourg, France) and were used without further purification. Source: (synth.) Escherichia coli (E. coli) / References: UniProt: P07017 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: Solution structure of AS1p-Tar in 10% negatively charged bicelles | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 50mM sodium phosphate; 240mM [U-2H] DHPC; 54mM [U-2H] DMPC; 6mM [U-2H] DMPG; 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.05 / pH: 7.2 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | ||||||||||||||||||||||||
NMR constraints | NOE constraints total: 133 / NOE intraresidue total count: 59 / NOE medium range total count: 33 / NOE sequential total count: 41 | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 25 / Maximum lower distance constraint violation: 0.15 Å / Maximum upper distance constraint violation: 0.19 Å / Representative conformer: 1 | ||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 1.04 Å / Distance rms dev error: 0.36 Å |